PREMADE PHAGE DIPLAY LIBRARIES

Unlock the Power of Phage Display With Our Premade Libraries

Phage display technology continues to play an important role in the selection and identification of peptides, monoclonal antibodies, and antibody fragments that exhibit binding affinity to specific target antigens. The technology is widely employed in the pharmaceutical industry, in which it facilitates the development of novel drugs, including peptide ligands and antibodies that target disease biomarkers. Furthermore, it is instrumental in immunology research, enabling comprehensive studies of antibody-antigen interactions. Phage display technology involves the creation of filamentous fusion phages that display random foreign peptides or antibodies on a viral coat protein. The phages are assembled into a library of peptides or antibodies, known as a phage display library.

Cell Origins carries premade linear and cyclic peptide phage display libraries. Additionally, our scientists will work directly with you to develop customized peptide and antibody phage display libraries with built-in selection and tagging strategies to meet your specific research needs.

Choosing the Right Phage Display Library

Peptide phage display technology is a powerful technique that can be used for a wide variety of applications in research and drug discovery. For example, peptides can be used directly as drugs to elicit therapeutic effects or to carry cargo to target biomarkers of disease. Antibody phage display libraries are similarly used in drug discovery and in many types of research methods. In fact, full-length monoclonal antibodies have become one of the most important classes of biopharmaceuticals.

Bacteriophage Vectors

The bacteriophage vectors encode a modified version of the full phage genome that contains an antibiotic selection gene, as well as a recombinant gene encoding the foreign peptide or antibody fused to one of the coat proteins. The large size of antibodies and antibody fragments impairs the infection of E. coli and thus often leave bacteriophage vectors unsuitable for the display of this type of ligands. However, bacteriophage vectors have been used successfully numerous times for peptide phage display on various coat proteins. Bacteriophage vectors do not require the use of helper phages for the propagation of viral particles since the phage genome contains all of the necessary genes for replication.

Phagemids

Phagemids are plasmid-based vectors that contain the phage and bacterial origins of replication as well as an antibiotic selection gene. Contrary to the bacteriophage vectors, phagemids do not contain most of the wild type genes of the filamentous phage. However, they typically encode a hybrid coat protein fused to a foreign full-length antibody, antibody fragment, nanobody, or peptide. Phagemid vectors can independently replicate in E. coli ; however they require a helper phage for the production of phage clones. The helper phage contain essential genes that are necessary for the assembly and release of phage particles. The relatively small size of phagemid DNA enables easy transformation of E. coli , which directly relates to the diversity of the phage display library. This property is therefore one of the most important considerations when choosing an appropriate vector for phage display. Finally, phagemid vectors can be used to display large ligands including full-length antibodies and antibody fragments.

Cell Origins carries bacteriophage and phagemid vectors based on the original vectors created by Dr. George Smith. Many of our vectors include built-in tagging options to streamline your phage display selections and screening procedures.

Linear Peptides

Both linear and cyclic peptide sequences can be selected using phage display technology and each has its distinct advantages and disadvantages. Linear phage display peptide libraries have been available for decades and are typically cheaper compared to their cyclic counterparts. Additionally, the synthesis of soluble linear peptides is most often easier and more cost-effective, making them a more convenient option for researchers. However, they can have limited bioavailability due to their rapid degradation in the body, which can limit their efficacy as a drug unless they are substantially modified.

Cyclic Peptides

Several novel phage display libraries of cyclic peptides have been developed over the last decade. Such phage-displayed peptide libraries are typically created by inducing disulfide bond formation between cysteine residues, or by using a scaffolding system. Cyclic peptides offer better stability due to their non-natural structure. They also typically offer higher target binding affinity and specificity as a result of their rigid structure. This makes them ideal for applications where high potency or selectivity is required.

Peptide Phage Display Libraries